Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QSG

CRYSTAL STRUCTURE OF ENOYL REDUCTASE INHIBITION BY TRICLOSAN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006633	biological_process	fatty acid biosynthetic process
A	0008610	biological_process	lipid biosynthetic process
A	0009102	biological_process	biotin biosynthetic process
A	0016020	cellular_component	membrane
A	0030497	biological_process	fatty acid elongation
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0051289	biological_process	protein homotetramerization
A	0070404	molecular_function	NADH binding
A	1902494	cellular_component	catalytic complex
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006633	biological_process	fatty acid biosynthetic process
B	0008610	biological_process	lipid biosynthetic process
B	0009102	biological_process	biotin biosynthetic process
B	0016020	cellular_component	membrane
B	0030497	biological_process	fatty acid elongation
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0051289	biological_process	protein homotetramerization
B	0070404	molecular_function	NADH binding
B	1902494	cellular_component	catalytic complex
C	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0006633	biological_process	fatty acid biosynthetic process
C	0008610	biological_process	lipid biosynthetic process
C	0009102	biological_process	biotin biosynthetic process
C	0016020	cellular_component	membrane
C	0030497	biological_process	fatty acid elongation
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0051289	biological_process	protein homotetramerization
C	0070404	molecular_function	NADH binding
C	1902494	cellular_component	catalytic complex
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0006633	biological_process	fatty acid biosynthetic process
D	0008610	biological_process	lipid biosynthetic process
D	0009102	biological_process	biotin biosynthetic process
D	0016020	cellular_component	membrane
D	0030497	biological_process	fatty acid elongation
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0051289	biological_process	protein homotetramerization
D	0070404	molecular_function	NADH binding
D	1902494	cellular_component	catalytic complex
E	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
E	0005515	molecular_function	protein binding
E	0005829	cellular_component	cytosol
E	0006633	biological_process	fatty acid biosynthetic process
E	0008610	biological_process	lipid biosynthetic process
E	0009102	biological_process	biotin biosynthetic process
E	0016020	cellular_component	membrane
E	0030497	biological_process	fatty acid elongation
E	0032991	cellular_component	protein-containing complex
E	0042802	molecular_function	identical protein binding
E	0051289	biological_process	protein homotetramerization
E	0070404	molecular_function	NADH binding
E	1902494	cellular_component	catalytic complex
F	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
F	0005515	molecular_function	protein binding
F	0005829	cellular_component	cytosol
F	0006633	biological_process	fatty acid biosynthetic process
F	0008610	biological_process	lipid biosynthetic process
F	0009102	biological_process	biotin biosynthetic process
F	0016020	cellular_component	membrane
F	0030497	biological_process	fatty acid elongation
F	0032991	cellular_component	protein-containing complex
F	0042802	molecular_function	identical protein binding
F	0051289	biological_process	protein homotetramerization
F	0070404	molecular_function	NADH binding
F	1902494	cellular_component	catalytic complex
G	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
G	0005515	molecular_function	protein binding
G	0005829	cellular_component	cytosol
G	0006633	biological_process	fatty acid biosynthetic process
G	0008610	biological_process	lipid biosynthetic process
G	0009102	biological_process	biotin biosynthetic process
G	0016020	cellular_component	membrane
G	0030497	biological_process	fatty acid elongation
G	0032991	cellular_component	protein-containing complex
G	0042802	molecular_function	identical protein binding
G	0051289	biological_process	protein homotetramerization
G	0070404	molecular_function	NADH binding
G	1902494	cellular_component	catalytic complex
H	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
H	0005515	molecular_function	protein binding
H	0005829	cellular_component	cytosol
H	0006633	biological_process	fatty acid biosynthetic process
H	0008610	biological_process	lipid biosynthetic process
H	0009102	biological_process	biotin biosynthetic process
H	0016020	cellular_component	membrane
H	0030497	biological_process	fatty acid elongation
H	0032991	cellular_component	protein-containing complex
H	0042802	molecular_function	identical protein binding
H	0051289	biological_process	protein homotetramerization
H	0070404	molecular_function	NADH binding
H	1902494	cellular_component	catalytic complex

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	80
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10201369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10398587","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10493822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10595560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11514139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12109908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12699381","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8953047","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Site: {"description":"Involved in acyl-ACP binding"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
A	TYR156
A	LYS163

site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
B	TYR156
B	LYS163

site_id	CSA3
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
C	TYR156
C	LYS163

site_id	CSA4
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
D	TYR156
D	LYS163

site_id	CSA5
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
E	TYR156
E	LYS163

site_id	CSA6
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
F	TYR156
F	LYS163

site_id	CSA7
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
G	TYR156
G	LYS163

site_id	CSA8
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 9878369

Chain	Residue	Details
H	TYR156
H	LYS163

site_id	MCSA1
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
A	TYR156	proton acceptor, proton donor
A	LYS163	electrostatic stabiliser

site_id	MCSA2
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
B	TYR156	proton acceptor, proton donor
B	LYS163	electrostatic stabiliser

site_id	MCSA3
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
C	TYR156	proton acceptor, proton donor
C	LYS163	electrostatic stabiliser

site_id	MCSA4
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
D	TYR156	proton acceptor, proton donor
D	LYS163	electrostatic stabiliser

site_id	MCSA5
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
E	TYR156	proton acceptor, proton donor
E	LYS163	electrostatic stabiliser

site_id	MCSA6
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
F	TYR156	proton acceptor, proton donor
F	LYS163	electrostatic stabiliser

site_id	MCSA7
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
G	TYR156	proton acceptor, proton donor
G	LYS163	electrostatic stabiliser

site_id	MCSA8
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
H	TYR156	proton acceptor, proton donor
H	LYS163	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)